Increased proteolytic susceptibility of carboxypeptidase Y caused by modification of the disulfide zipper

Biosci Biotechnol Biochem. 2002 Jun;66(6):1393-5. doi: 10.1271/bbb.66.1393.

Abstract

To investigate the structural importance of a "disulfide zipper" motif of carboxypeptidase Y, disulfide-deficient mutant enzymes were expressed in two strains of Saccharomyces cerevisiae. The mutant enzymes were rapidly degraded into fragments by intracellular proteases. Thus, it is concluded that the disulfide zipper is essential in maintaining the structural integrity of CPase Y against proteolytic susceptibility.

MeSH terms

  • Blotting, Western
  • Carboxypeptidases / chemistry*
  • Carboxypeptidases / genetics
  • Carboxypeptidases / metabolism*
  • Cathepsin A
  • Disulfides / chemistry
  • Disulfides / metabolism
  • Endopeptidases / metabolism*
  • Enzyme Stability
  • Mutation / genetics
  • Protein Conformation
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics

Substances

  • Disulfides
  • Carboxypeptidases
  • Endopeptidases
  • Cathepsin A